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GC_VZVD
ID   GC_VZVD                 Reviewed;         591 AA.
AC   P09256; P10241;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   02-JUN-2021, entry version 93.
DE   RecName: Full=Envelope glycoprotein C;
DE            Short=gC;
DE   AltName: Full=Glycoprotein V;
DE            Short=gpV;
GN   Name=gC; ORFNames=14;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Scott;
RX   PubMed=3016329; DOI=10.1128/jvi.59.3.660-668.1986;
RA   Kinchington P.R., Remenick J., Ostrove J.M., Straus S.E., Ruyechan W.T.,
RA   Hay J.;
RT   "Putative glycoprotein gene of varicella-zoster virus with variable copy
RT   numbers of a 42-base-pair repeat sequence has homology to herpes simplex
RT   virus glycoprotein C.";
RL   J. Virol. 59:660-668(1986).
CC   -!- FUNCTION: Essential for the initial attachment to heparan sulfate
CC       moieties of the host cell surface proteoglycans. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein C family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-32 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA27897.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X04370; CAA27897.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M13795; AAA69563.1; -; Genomic_DNA.
DR   PIR; E27342; VGBE14.
DR   PRIDE; P09256; -.
DR   Proteomes; UP000002602; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039573; P:suppression by virus of host complement activation; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR001038; GA_GC.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF02124; Marek_A; 1.
DR   PRINTS; PR00668; GLYCPROTEINC.
DR   SUPFAM; SSF48726; SSF48726; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Host-virus interaction;
KW   Inhibition of host complement factors by virus; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix;
KW   Viral attachment to host adhesion receptor; Viral attachment to host cell;
KW   Viral immunoevasion; Virion; Virus entry into host cell.
FT   CHAIN           1..591
FT                   /note="Envelope glycoprotein C"
FT                   /id="PRO_0000115762"
FT   TOPO_DOM        1..561
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        562..582
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        583..591
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          70..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        189..207
FT                   /evidence="ECO:0000250"
FT   DISULFID        374..436
FT                   /evidence="ECO:0000250"
FT   DISULFID        475..533
FT                   /evidence="ECO:0000250"
FT   DISULFID        479..507
FT                   /evidence="ECO:0000250"
FT   VARIANT         26
FT                   /note="V -> G (in strain: Scott)"
FT   VARIANT         96
FT                   /note="S -> T (in strain: Scott)"
FT   VARIANT         124
FT                   /note="T -> S (in strain: Scott)"
FT   VARIANT         138
FT                   /note="S -> T (in strain: Scott)"
FT   VARIANT         154
FT                   /note="K -> N (in strain: Scott)"
FT   VARIANT         166
FT                   /note="S -> T (in strain: Scott)"
FT   VARIANT         175
FT                   /note="T -> A (in strain: Scott)"
FT   VARIANT         184
FT                   /note="Y -> F (in strain: Scott)"
SQ   SEQUENCE   591 AA;  64862 MW;  A0104C906019D589 CRC64;
     MSKKTFPSFK FRGGCFNLLF KGSVDVSIKT RMKRIQINLI LTIACIQLST ESQPTPVSIT
     ELYTSAATRK PDPAVAPTSA ASRKPDPAVA PTSAASRKPD PAVAPTSAAS RKPDPAVAPT
     SAATRKPDPA VAPTSAASRK PDPAVAPTSA ATRKPDPAVA PTSAASRKPD PAANTQHSQP
     PFLYENIQCV HGGIQSIPYF HTFIMPCYMR LTTGQQAAFK QQQKTYEQYS LDPEGSNITR
     WKSLIRPDLH IEVWFTRHLI DPHRQLGNAL IRMPDLPVML YSNSADLNLI NNPEIFTHAK
     ENYVIPDVKT TSDFSVTILS MDATTEGTYI WRVVNTKTKN VISEHSITVT TYYRPNITVV
     GDPVLTGQTY AAYCNVSKYY PPHSVRVRWT SRFGNIGKNF ITDAIQEYAN GLFSYVSAVR
     IPQQKQMDYP PPAIQCNVLW IRDGVSNMKY SAVVTPDVYP FPNVSIGIID GHIVCTAKCV
     PRGVVHFVWW VNDSPINHEN SEITGVCDQN KRFVNMQSSC PTSELDGPIT YSCHLDGYPK
     KFPPFSAVYT YDASTYATTF SVVAVIIGVI SILGTLGLIA VIATLCIRCC S
 
 
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